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Database: UniProt
Entry: A0A0R0DED6_9GAMM
LinkDB: A0A0R0DED6_9GAMM
Original site: A0A0R0DED6_9GAMM 
ID   A0A0R0DED6_9GAMM        Unreviewed;      1147 AA.
AC   A0A0R0DED6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=ABB28_02375 {ECO:0000313|EMBL:KRG76663.1};
OS   Stenotrophomonas chelatiphaga.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas.
OX   NCBI_TaxID=517011 {ECO:0000313|EMBL:KRG76663.1, ECO:0000313|Proteomes:UP000051386};
RN   [1] {ECO:0000313|EMBL:KRG76663.1, ECO:0000313|Proteomes:UP000051386}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21508 {ECO:0000313|EMBL:KRG76663.1,
RC   ECO:0000313|Proteomes:UP000051386};
RA   Patil P.P., Midha S., Patil P.B.;
RT   "Genome sequencing and analysis of members of genus Stenotrophomonas.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the sodium:solute symporter (SSF) (TC 2.A.21)
CC       family. {ECO:0000256|ARBA:ARBA00006434}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRG76663.1}.
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DR   EMBL; LDJK01000007; KRG76663.1; -; Genomic_DNA.
DR   RefSeq; WP_057507079.1; NZ_LDJK01000007.1.
DR   AlphaFoldDB; A0A0R0DED6; -.
DR   PATRIC; fig|517011.3.peg.2831; -.
DR   Proteomes; UP000051386; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   CDD; cd00075; HATPase; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   CDD; cd00156; REC; 1.
DR   CDD; cd10322; SLC5sbd; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 1.
DR   Gene3D; 1.20.1730.10; Sodium/glucose cotransporter; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR003661; HisK_dim/P.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR038377; Na/Glc_symporter_sf.
DR   InterPro; IPR001734; Na/solute_symporter.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   NCBIfam; NF041832; near_NosP_CTERM; 1.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR43047:SF9; HISTIDINE KINASE; 1.
DR   PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF12860; PAS_7; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00091; PAS; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50283; NA_SOLUT_SYMP_3; 1.
DR   PROSITE; PS50112; PAS; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000051386};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        35..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        66..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        115..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        153..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        187..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        233..251
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        272..299
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        319..352
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        373..392
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        404..425
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        437..454
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          633..670
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          788..1002
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          1029..1143
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         1077
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1147 AA;  125888 MW;  48E630FAD003635D CRC64;
     MSSWILLLVS VAYAALLFGV AWWGDRRPLY PDRPWLRPVV YSLALAVYCS SWTFYGAVGT
     AVRSGIGYLS IYVGPLLMML FGWRIIERLA LVARSQNVVS IADFISSRFG RSRRLAALVA
     IIALIGVVPY LALQYKAVAM SLQVLTGDSG PTGYFSDPAL YVALLMALFA TLFGTRQVDA
     TEHHHGMMLA IALESVIKLL AMVAVGVFAY LWLSERTDAV VQSAHTLFTS LPPVGFISQT
     LLSFLAIVCL PRQFHVAVVE CGDVRDVRRA RWMFGGYLVV ISAMVIPIAT AGVTLFGTGG
     TVADDAMVLA LPLHEGRNAL ALIAYVGGFS AATGMVIVSS IALATMISND LVMPVLLRRS
     GGTGEAADVA SRVLWIRRLA ILFLALIAYT YYRSSGNDNS LASYGLMAFA AVAQFAPGLI
     GGLYWRGASR RGVETGIVLG FATWIYTLLL PALTQSGLLD AGWLNEGPFG VAWLRPQQLF
     GMSGWDPLTH GTFWSLLVNA ATMMLVSARW RPSVDERLRA APFLDPYAQR PSVASGWPGH
     VHVGDLLALA SRVVGERHAR RSFFEQAQSL GRELQTQVPA DRPWVQFTER LLAASIGAAS
     ARLLLTSLLR GSGMDLGEVV AVLDEAGQEL RFNREILSTT LENISAGVSV VDPDMRLTAW
     NRRYQDMFGY PDGMLYVGRP VADLIRYNAE RGELGEGEIE RQISRRIRYM RAGSPHVFER
     TRSDGKVIEM RGQALPGGGY VTSYNDITDY KHAEKALLEA NETLEQRVAE RSNAAEAAQQ
     SKTRFLAAIS HDVLQPLNAA RLFASALRES HHNNEEQRHL AERVDASLRA AEELLDGLLD
     VSRLDAGGLH PVIGEFDASA LMRELAAQYS PVAAGRGLRL DLFARPAWVR SDRRLLRRVM
     QNFLANALRY TRQGRIVLAV RLRGNEVELQ VWDTGPGIPE HHMQQIFDEF HRYQQPFDWG
     EQGLGLGLSI CQRISRLLDH RLNARSRVGS GSMFSIALPR VAATPGASEQ ELMAAAPAAV
     RADSLAGMRV LCVDNDEEIL DGMRALLGRW QVQVITASTV DQALEKMAEH PDVMLVDYHL
     HDRLDGLDTL VALREAAGSD LPGALLTADG RDELKRMARD RGYRLLTKPI KPASLRAFLA
     AYATPRD
//
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